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238 results on '"Stura, E."'

2. Structural and functional properties of the Kunitz-type and C-terminal domains of Amblyomin-X supporting its antitumor activity

Author

Morais, K. L. P., primary, Ciccone, L., additional, Stura, E., additional, Alvarez-Flores, M. P., additional, Mourier, G., additional, Driessche, M. Vanden, additional, Sciani, J. M., additional, Iqbal, A., additional, Kalil, S. P., additional, Pereira, G. J., additional, Marques-Porto, R., additional, Cunegundes, P., additional, Juliano, L., additional, Servent, D., additional, and Chudzinski-Tavassi, A. M., additional

Published
2023
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8. A B-Cell Superantigen that Targets B-1 Lymphocytes

Author

Silverman, G. J., primary, Cary, S., additional, Graille, M., additional, Curtiss, V. E., additional, Wagenknech, R., additional, Luo, L., additional, Dwyer, D., additional, Goodyear, C., additional, Corper, A. L., additional, Stura, E. A., additional, and Charbonnier, J. -B., additional

Published
2000
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10. A peptide mimetic as antigen and immunogen

Author

Satterthwait, Arnold C., primary, Cabezas, Edelmira, additional, Calvo, Julio C., additional, Chen, Shao-Qing, additional, Wu, Jia-Xiang, additional, Wang, Peng-Liang, additional, Xie, Yi-Ling, additional, Stura, E. A., additional, and Kaslow, D. C., additional

Published
1995
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23. Structure-based secondary structure-independent approach to design protein ligands: Application to the design of Kv1.2 Potassium channel blockers

Author

Magis, C., Gasparini, D., Lecoq, A., Du, Le M.H., Stura, E., Charbonnier, J.B., Mourier, G., Boulain, J.C., Pardo, L., Caruana, A., Joly, A., Lefranc, M., Masella, M., Menez, A., and Cuniasse, P.

Subjects
Protein binding -- Research, Amino acids -- Research, Proteins -- Structure, Proteins -- Research, Chemistry
Abstract

A structure-based approach to the design of protein ligands was developed, based on the transfer of a functional binding motif of amino acids on a host protein able to reproduce the functional topology of the residues. The results of the experiment showed that protein ligands have binding results consistent with the presumed binding mode.

Published
2006

24. N-O-Isopropyl Sulfonamido-Based Hydroxamates as Matrix Metalloproteinase Inhibitors: Hit Selection and in Vivo Antiangiogenic Activity

Author

Nuti, E, Cantelmo, A, Gallo, C, Bruno, A, Bassani, B, Camodeca, C, Tuccinardi, T, Vera, L, Orlandini, E, Nencetti, S, Stura, E, Martinelli, A, Dive, V, Albini, A, Rossello, A, Nuti E, Cantelmo AR, Gallo C, Bruno A, Bassani B, Camodeca C, Tuccinardi T, Vera L, Orlandini E, Nencetti S, Stura EA, Martinelli A, Dive V, Albini A, Rossello A, Nuti, E, Cantelmo, A, Gallo, C, Bruno, A, Bassani, B, Camodeca, C, Tuccinardi, T, Vera, L, Orlandini, E, Nencetti, S, Stura, E, Martinelli, A, Dive, V, Albini, A, Rossello, A, Nuti E, Cantelmo AR, Gallo C, Bruno A, Bassani B, Camodeca C, Tuccinardi T, Vera L, Orlandini E, Nencetti S, Stura EA, Martinelli A, Dive V, Albini A, and Rossello A

Abstract

Matrix metalloproteinases (MMPs) have been shown to be involved in tumor-induced angiogenesis. In particular, MMP-2, MMP-9, and MMP-14 have been reported to be crucial for tumor angiogenesis and the formation of metastasis, thus becoming attractive targets in cancer therapy. Here, we report our optimization effort to identify novel N-isopropoxy-arylsulfonamide hydroxamates with improved inhibitory activity toward MMP-2, MMP-9, and MMP-14 with respect to the previously discovered compound 1. A new series of hydroxamates was designed, synthesized, and tested for their antiangiogenic activity using in vitro assays with human umbilical vein endothelial cells (HUVECs). A nanomolar MMP-2, MMP-9, and MMP-14 inhibitor was identified, compound 3, able to potently inhibit angiogenesis in vitro and also in vivo in the matrigel sponge assay in mice. Finally, X-ray crystallographic and docking studies were conducted for compound 3 in order to investigate its binding mode to MMP-9 and MMP-14.

Published
2015

26. Third generation of matrix metalloprotease inhibitors: Gain in selectivity by targeting the depth of the S1' cavity

Author

Devel, L. Czarny, B. Beau, F. Georgiadis, D. Stura, E. Dive Vincent, V.

Abstract

Following the disappointment of clinical trials with early broad-spectrum synthetic inhibitors of matrix metalloproteases (MMPs), the field is now resurging with a new focus on the development of more selective inhibitors. Compounds able to fully discriminate between different members of the MMP family are sorely needed for therapeutic applications. Chemical efforts over the past years have led to very few selective inhibitors of MMPs. The over-exploitation of the hydroxamate function, or other strong zinc-binding groups, might be responsible for this failure. By resorting to weaker zinc-chelating groups, like phosphoryl or carboxylic groups, inhibitors with improved selectivity profiles have been developed. However, the most encouraging results have been obtained with compounds that avoid targeting the zinc but gain their affinity from plunging deeper into the MMP S1' cavity. Analyses of the crystal structures of MMP-13 and MMP-8 complexes with such compounds provide novel insights for the design of more selective inhibitors for other members of the MMP family. © 2010 Elsevier Masson SAS.

Published
2010

28. Insights from selective non-phosphinic inhibitors of MMP-12 tailored to fit with an S1′ loop canonical conformation

Author

Devel, L. Garcia, S. Czarny, B. Beau, F. Lajeunesse, E. Vera, L. Georgiadis, D. Stura, E. Dive, V.

Abstract

After the disappointment of clinical trials with early broad spectrum synthetic inhibitors of matrix metalloproteinases (MMPs), the field is now resurging with a new focus on the development of selective inhibitors that fully discriminate between different members of the MMP family with several therapeutic applications in perspective. Here, we report a novel class of highly selective MMP-12 inhibitors, without a phosphinic zinc-binding group, designed to plunge deeper into the S1′ cavity of the enzyme. The best inhibitor from this series, identified through a systematic chemical exploration, displays nanomolar potency toward MMP-12 and selectivity factors that range between 2 and 4 orders of magnitude toward a large set of MMPs. Comparison of the high resolution x-ray structures of MMP-12 in free state or bound to this new MMP-12 selective inhibitor reveals that this compound fits deeply within the S1′ specificity cavity, maximizing surface/volume ratios, without perturbing the S1′ loop conformation. This is in contrast with highly selective MMP-13 inhibitors that were shown to select a particular S1′ loop conformation. The search for such compounds that fit precisely to preponderant S 1′ loop conformation of a particular MMP may prove to be an alternative effective strategy for developing selective inhibitors of MMPs. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.

Published
2010

34. Sensore per gas acidi

Author

Carrara, S, Stura, E, Bavastrello, V, and Nicolini, Claudio

Published
2003

35. Structural evidences for a functional rôle of human tissue non-specific alkaline phosphatase in bone mineralization

Author

Mornet, E., STURA, E., Lia-Baldini, Anne-Sophie, STIGBRAND, T., Menez, A., LE DU, M.H., Unité de Génétique Moléculaire Animale (UGMA), Université de Limoges (UNILIM)-Institut National de la Recherche Agronomique (INRA), Unité de Génétique Moléculaire Animale (UMR GMA), and Institut National de la Recherche Agronomique (INRA)-Université de Limoges (UNILIM)

Subjects
MEN, BONE, [SDV]Life Sciences [q-bio], tissu osseux, homme
Abstract

absent

Published
2001

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